GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com


Jump to: navigation, search

Sturany, S, Van Lint, J, Muller, F, Wilda, M, Hameister, H, Hocker, M, Brey, A, Gern, U, Vandenheede, J, Gress, T, Adler, G and Seufferlein, T (2001) Molecular cloning and characterization of the human protein kinase D2. A novel member of the protein kinase D family of serine threonine kinases. J. Biol. Chem. 276:3310-8


We have isolated the full-length cDNA of a novel human serine threonine protein kinase gene. The deduced protein sequence contains two cysteine-rich motifs at the N terminus, a pleckstrin homology domain, and a catalytic domain containing all the characteristic sequence motifs of serine protein kinases. It exhibits the strongest homology to the serine threonine protein kinases PKD/PKCmicro and PKCnu, particularly in the duplex zinc finger-like cysteine-rich motif, in the pleckstrin homology domain and in the protein kinase domain. In contrast, it shows only a low degree of sequence similarity to other members of the PKC family. Therefore, the new protein has been termed protein kinase D2 (PKD2). The mRNA of PKD2 is widely expressed in human and murine tissues. It encodes a protein with a molecular mass of 105 kDa in SDS-polyacrylamide gel electrophoresis, which is expressed in various human cell lines, including HL60 cells, which do not express PKCmicro. In vivo phorbol ester binding studies demonstrated a concentration-dependent binding of [(3)H]phorbol 12,13-dibutyrate to PKD2. The addition of phorbol 12,13-dibutyrate in the presence of dioleoylphosphatidylserine stimulated the autophosphorylation of PKD2 in a synergistic fashion. Phorbol esters also stimulated autophosphorylation of PKD2 in intact cells. PKD2 activated by phorbol esters efficiently phosphorylated the exogenous substrate histone H1. In addition, we could identify the C-terminal Ser(876) residue as an in vivo phosphorylation site within PKD2. Phosphorylation of Ser(876) of PKD2 correlated with the activation status of the kinase. Finally, gastrin was found to be a physiological activator of PKD2 in human AGS-B cells stably transfected with the CCK(B)/gastrin receptor. Thus, PKD2 is a novel phorbol ester- and growth factor-stimulated protein kinase.


PubMed Online version:10.1074/jbc.M008719200


Amino Acid Sequence; Carcinogens/pharmacology; Cells, Cultured; Cloning, Molecular; DNA, Complementary/analysis; DNA, Complementary/genetics; Enzyme Activation; Growth Substances/pharmacology; HL-60 Cells; Humans; Molecular Sequence Data; Molecular Weight; Phorbol 12,13-Dibutyrate/pharmacology; Phorbol Esters/pharmacology; Phosphorylation; Protein Kinases/chemistry; Protein Kinases/drug effects; Protein Kinases/genetics; Protein Kinases/metabolism; Sequence Homology, Amino Acid; Serine/metabolism; Signal Transduction/physiology; Transfection; Tritium



Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status



GO:0006468: protein phosphorylation

ECO:0000303: author statement without traceable support used in manual assertion


Seeded From UniProt




GO:0004674: protein serine/threonine kinase activity

ECO:0000303: author statement without traceable support used in manual assertion


Seeded From UniProt


See also


See Help:References for how to manage references in GONUTS.